Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation

Abstract

Supplemental Digital Content is available in the text

The challenges of glycan recognition with natural and artificial receptors

“…General information about the glycosylation pattern can be determined, such as whether it is N-glycosylated, O-glycosylated, high mannose, core fucosylated, and fully or partially sialylated, with potential applications in the development of disease-related biomarkers. 11,87,[89][90][91] Despite the benefits associated with lectin microarrays, the inherent low affinity and specificity of lectins hinder their detection performances. In order to improve their binding properties, researchers have started to focus their efforts on lectin engineering.…”

Enveloped Viruses: Pathogenetic Targets for Cyanobacterial Lectins

“…Lectins from algae and cyanobacteria effectively inhibit HCV, but the toxic and immunogenic effects of these compounds do not allow presenting them as drugs so far. However, the HCV life cycle is highly conserved and may be a suitable target for antiviral therapy [92].…”

“…Лектины из водорослей и цианобактерий достаточно эффективно ингибируют HCV, однако токсическое и иммуногенное действие этих соединений до настоящего времени не позволяют представить их в качестве лекарственных средств. Вместе с тем жизненный цикл HCV отличается высокой консервативностью и может быть подходящей мишенью для противовирусной терапии [92].…”

Hepatitis C Virus Glycan-Dependent Interactions and the Potential for Novel Preventative Strategies

“…Lectin microarray exploits the binding specificity of a panel of lectins (glycan-binding proteins) to detect the presence of specific glycan epitopes, thus enabling the precise identification of partial glycan structures. A lectin microarray screen with HCVcc glycoproteins identified high mannose type N-glycans as the predominant glycoforms, followed by hybrid/complex type N-glycans [35]. The identified complex Nglycan glycoforms were highly heterogeneous, including abundant sialylation, fucosylation, and bisecting N-acetylglucosamine (GlcNAc).…”

“…The 16 distinct N-glycans identified on HCVcc virions by MS were mostly consistent with the results from the lectin microarray. The microarray screen identified 10 lectins that bound to glycoproteins bearing terminal galactose (Gal) or N-acetylgalactosamine (GalNAc) residues, whereas MS identified one structure that was a mono-galactosylated N-glycan [35]. This suggests that the lectin binding to Gal/GalNAc-containing glycans may recognize O-glycans bearing these epitopes, although this has not been fully investigated.…”